ELISA detection of IgG and IgM antibodies to spike glycoprotein (E1), nucleoprotein (NP) and virus-like particles (VLP) of Rubella virus.
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RUBELLA VIRUS VLP
Rubella virus-like particles are produced by recombinant expression of Rubella structural polyprotein (amino acids 1-1063, Uniprot accession number NP_062884.1) in HEK293 cells.
PRODUCT DETAILS – RUBELLA VIRUS VLP
- Recombinant Rubella virus-like particles comprising Spike glycoprotein E1, Spike glycoprotein E2 and Capsid protein expressed from HEK293 cells (strain F-Therien, NCBI Accession Number: NP_062884.1).
- Greater than 95% purity by SDS-PAGE and buffered in 40mM TRIS-HCl pH8.0, 100mM NaCl.
- Chaye, H. et al., 1992. Localization of the virus neutralizing and hemagglutinin epitopes of E1 glycoprotein of rubella virus. Virology , Volume 189, p. 483–492.
- Green, K. Y. & Dorsett, P. H., 1986. Rubella virus antigens: localization of epitopes involved in hemagglutination and neutralization by using monoclonal antibodies. J. Virol., Volume 57, p. 893–898.
- Oker-Blom, C., Kalkkinen, N., Kääriäinen, L. & Pettersson, R., 1983. Rubella virus contains one capsid protein and three envelope glycoproteins, E1, E2a, and E2b. J. Virol., Volume 964–973, p. 964–973.
- Qiu, Z., Ou, D., Hobman, T. C. & Gillam, S., 1994. Expression and characterization of virus-like particles containing rubella virus structural proteins. Journal of Virology, 68(6), pp. 4086-4091.
- Wolinsky, J. S. et al., 1983. An antibody- and synthetic peptide-defined rubella virus E1 glycoprotein neutralization domain. J. Virol., Volume 67, p. 961–968.
- Yang, D., Hwang, D., Zhiyong, Q. & Gillam, S., 1998. Effects of Mutations in the Rubella Virus E1 Glycoprotein on E1-E2 Interaction and Membrane Fusion Activity. J Virol., 72(11), p. 8747–8755.
BACKGROUND
Rubella virus is an enveloped, positive single-stranded RNA virus and a member of the genus Rubivirus, which belongs to the Togaviridae family. It consists of three structural proteins: a capsid protein and two membrane-spanning glycoproteins, E1 and E2, localized in the virus envelope (Oker-Blom, et al., 1983).
E1 and E2 exist as a heterodimer and form the viral spike complexes on the virion surface. Formation of an E1-E2 heterodimer is required for transport of E1 out of the endoplasmic reticulum lumen to the Golgi apparatus and plasma membrane (Yang, et al., 1998). E1 is the dominant surface molecule of the virus particle representing the main target for the detection and subsequent elimination of virus by the host’s immune system (Green & Dorsett, 1986; Wolinsky, et al., 1983). Although both E1 and E2 provide lifelong immunity, hemagglutination (HA) and viral neutralization (VN) is believed to be mainly targeted to E1 protein epitopes (Chaye, et al., 1992).
Immunogenicity studies have shown Rubella VLPs to be significantly more active than soluble E1 protein in inducing antibody responses in mice, especially for producing VN and HA-inhibiting activity. VLPs have also been shown to stimulate cell-mediated immune responses to Rubella virus and Rubella virus structural proteins, which may be important in providing protective immunity against infection. Therefore, VLPs show good potential for safe vaccine development (Qiu, et al., 1994).
REFERENCES
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颗粒型抗原,除了有细菌、红细胞、螺旋体等天然颗粒型抗原,还有吸附有可溶性抗原的非免疫相关颗粒.
颗粒性抗原光镜下可见,比如细菌性抗原、红细胞抗原等;而可溶性抗原在光镜下不可见,如组织浸出液、细菌毒素、蛋白质分子等。
它们不等同于完全抗原和不完全抗原。完全抗原具有免疫原性和抗原性,而不完全抗原只具有抗原性。完全抗原可以是颗粒性抗原,亦可是可溶性抗原,而不完全抗原一般只能是可溶性抗原,不会是颗粒性抗原。
荚膜是某些细菌在细胞壁外包围的一层粘液性物质,一般由糖和多肽组成,是细菌的一种特殊结构。
作用:
①抗吞噬作用:荚膜因其亲水性及其空间占位、屏障作用,可有效抵抗寄主吞噬细胞的吞噬作用。
②黏附作用:荚膜多糖可使细菌彼此间粘连,也可黏附于组织细胞或无生命物体表面,是引起感染的重要因素,具有荚膜的S-型肺炎链球菌毒力强,有助于肺炎链球菌侵染人体;废水生物处理中的细菌荚膜有生物吸附作用,将废水中的有机物、无机物及胶体吸附在细菌体表面上。
③抗有害物质的损伤作用:处于细菌细胞最外层,荚膜犹如盔甲可有效保护菌体免受或少受多种杀菌、抑菌物质的损伤,如溶菌酶、补体等。
④抗干燥作用:荚膜多糖为高度水合分子,含水量在95%以上,可帮助细菌抵抗干燥对生存的威胁。
⑤当缺乏营养时,荚膜可被利用作碳源和能源,有的荚膜还可作氮源。
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